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Enzyme Nomenclature
Information on EC 2.3.1.110 - tyramine N-feruloyltransferase
Word Map on EC 2.3.1.110
- 2.3.1.110
- amide
-
wound
- tobacco
- octopamine
- potato
-
hydroxycinnamic
-
pepper
- l-tyrosine
- noradrenaline
- annuum
- capsicum
-
plant-specific
-
caffeoyl
-
elicitor
- sinapoyl-coa
-
multigene
-
4.1.1.25
-
nicotiana
- serotonin
- l-phenylalanine
- tabacum
- syringae
-
cell-suspension
-
xanthi
- nutrition
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.3.1.110
-
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RECOMMENDED NAME
GeneOntology No.
tyramine N-feruloyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
feruloyl-CoA + tyramine = CoA + N-feruloyltyramine
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
feruloyl-CoA:tyramine N-(hydroxycinnamoyl)transferase
Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as donors, and some aromatic amines can act as acceptors.
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CAS REGISTRY NUMBER
COMMENTARY
128909-19-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
constitutive expression of enzyme, endogenous enzyme activity is wound-induced. Elevated enzyme activity reduces cellular tyramine levels
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
transgenic tomato plants overexpressing tomato hydroxycinnamoyl-CoA:tyramine N-hydroxycinnamoyl transferase THT display enhanced THT gene expression in leaves as compared with wild-type plants. Leaves, flowers and fruits of THT-overexpressing plants show a higher constitutive accumulation of the amide coumaroyltyramine. Feruloyltyramine also accumulates in these tissues. Accumulation of coumaroyltyramine, feruloyltyramine, ctopamine, and noradrenaline hydroxycinnamic acid amides in response to Pseudomonas syringae pv. tomato infection is higher in transgenic plants. Transgenic plants show an enhanced resistance to the bacterial infection. The hydroxycinnamic acid amides accumulation is accompanied by an increase in salicylic acid levels and pathogenesis-related gene induction
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + octopamine
CoA + N-(4-coumaroyl)octopamine
-
-
-
?
4-coumaroyl-CoA + phenethylamine
CoA + N-(4-coumaroyl)phenethylamine
-
-
-
?
4-coumaroyl-CoA + tryptamine
CoA + N-(4-coumaroyl)tryptamine
-
-
-
?
caffeoyl-CoA + tryptamine
CoA + N-caffeoyltryptamine
-
tryptamine at 17% the rate of phenylethylamine
-
-
?
feruloyl-4'-phosphopantetheine + tyramine
4'-phosphopantetheine + feruloyltyramine
-
-
-
-
?
feruloyl-CoA + (4-hydroxyphenyl)propylamine
CoA + feruloyl-(4-hydroxyphenyl)propylamine
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-
-
-
?
feruloyl-CoA + 3'-methoxyoctopamine
CoA + feruloyl-3'-methoxyoctopamine
-
-
-
?
feruloyl-CoA + 3-methoxytyramine
CoA + feruloyl-3-methoxytyramine
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-
-
-
?
feruloyl-CoA + beta-phenylethylamine
CoA + feruloyl-beta-phenylethylamine
-
-
-
-
?
feruloyl-CoA + N-methyltyramine
CoA + N-feruloyl-N-methyltyramine
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-
-
-
?
4-coumaroyl-CoA + tyramine
CoA + N-(4-coumaroyl)tyramine
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tyramine at 19% the rate of phenylethylamine
-
-
?
4-coumaroyl-CoA + tyramine
CoA + N-(4-coumaroyl)tyramine
-
-
-
?
4-coumaroyl-CoA + tyramine
CoA + N-(4-coumaroyl)tyramine
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-
i.e. 4-hydroxycinnamoyltyramine
?
4-coumaroyl-CoA + tyramine
CoA + N-(4-coumaroyl)tyramine
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-
i.e. 4-hydroxycinnamoyltyramine
?
caffeoyl-CoA + serotonin
CoA + N-caffeoylserotonin
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serotonin at 22% the rate of phenylethylamine
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-
?
caffeoyl-CoA + tyramine
CoA + N-caffeoyltyramine
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caffeoyl-CoA at 89% the rate of 4-coumaroyl-CoA
-
-
?
cinnamoyl-CoA + tyramine
CoA + cinnamoyltyramine
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cinnamoyl-CoA at 66% the rate of 4-coumaroyl-CoA
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-
?
feruloyl-CoA + dopamine
CoA + feruloyldopamine
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feruloyl-CoA at 20% the rate of 4-coumaroyl-CoA, dopamine at 27% the rate of phenylethylamine
-
-
?
feruloyl-CoA + noradrenaline
CoA + feruloylnoradrenaline
-
synonym: norepinephrine
-
-
?
feruloyl-CoA + tyramine
CoA + feruloyltyramine
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-
mainly the trans-form is produced, only traces of the cis-form can be found
?
feruloyl-CoA + tyramine
CoA + feruloyltyramine
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low specificity for cinnamoyl-CoA derivates and hydroxyphenethylamines
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?
additional information
?
-
wild-type enzyme shows no activity with serotonin, mutant enzyms F145Y and F145Y/Y147F show activity with serotonin
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-
-
additional information
?
-
recombinant LaAAT1 exhibits a broad substrate tolerance accepting (hydroxy)cinnamoyl-CoAs as acyl donors and not only tyramine, tryptamine, phenylethylamine, and anthranilic acid but also shikimic acid and 4-hydroxyphenyllactic acid as acceptors, showing substrate promiscuity
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-
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additional information
?
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substrate specificity of recombinant AAT1, overview. No or poor activity with anthranilic acid
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-
additional information
?
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enzyme has a wide specificity for phenylethylamines and cinnamoyl-CoA thioesters but differs in the affinity for the substrate, thus indicating different isoenzymes
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-
-
additional information
?
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enzyme has a wide specificity for phenylethylamines and cinnamoyl-CoA thioesters but differs in the affinity for the substrate, thus indicating different isoenzymes
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-
additional information
?
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enzyme exerts control over the flux of intermediates involved in hydroxycinnamic acid amide of tyramine under some conditions
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-
-
additional information
?
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tyraminehydroxycinnamoyl transferase is directly implicated in the formation of hydroxycinnamic acid amides
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Q0GA14
recombinant LaAAT1 exhibits a broad substrate tolerance accepting (hydroxy)cinnamoyl-CoAs as acyl donors and not only tyramine, tryptamine, phenylethylamine, and anthranilic acid but also shikimic acid and 4-hydroxyphenyllactic acid as acceptors, showing substrate promiscuity
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-
-
additional information
?
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-
enzyme exerts control over the flux of intermediates involved in hydroxycinnamic acid amide of tyramine under some conditions
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-
-
additional information
?
-
Q8H9D9
tyraminehydroxycinnamoyl transferase is directly implicated in the formation of hydroxycinnamic acid amides
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-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-hydroxyphenyl)amino sulfinyl acetic acid 1,1-dimethyl ester
-
i.e. OH-PAS, rapid inhibition, feruloyl-CoA prevents partially
diethyldicarbonate
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90% loss of activity after 5 min at 0.5 mM, preincubation with feruloyl-CoA protects
L-tyrosine beta-naphthylamide
-
competitive with respect to tyramine, reversible in the presence of high concentrations of tyramine
L-tyrosine beta-naphthylamide
-
competitive with respect to tyramine, reversible in the presence of high concentrations of tyramine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.057
4-Coumaroyl-CoA
with tyramine, pH 7.5, 30°C, recombinant AAT1
0.157
4-Coumaroyl-CoA
with tryptamine, pH 7.5, 30°C, recombinant AAT1
0.3
4-Coumaroyl-CoA
with phenethylamine, pH 7.5, 30°C, recombinant AAT1
0.326
caffeoyl-CoA
with tyramine, pH 7.5, 30°C, recombinant AAT1
0.49
cinnamoyl-CoA
with tyramine, pH 7.5, 30°C, recombinant AAT1
0.192
Feruloyl-CoA
with tyramine, pH 7.5, 30°C, recombinant AAT1
0.112
phenethylamine
with 4-coumaroyl-CoA, pH 7.5, 30°C, recombinant AAT1
0.005
tyramine
with caffeoyl-CoA, pH 7.5, 30°C, recombinant AAT1
0.018
tyramine
with cinnamoyl-CoA, pH 7.5, 30°C, recombinant AAT1
0.036
tyramine
with 4-coumaroyl-CoA, pH 7.5, 30°C, recombinant AAT1
0.045 - 0.07
tyramine
-
+ p-coumaroyl-CoA, depending on the enzyme fraction used
0.0588 - 0.071
tyramine
-
+ feruloyl-CoA, depending on the enzyme fraction used
0.17
tyramine
-
30°C, pH 8.5, mutant enzyme F145Y; 30°C, pH 8.5, mutant enzyme F145Y/Y147F
0.243
tyramine
with feruloyl-CoA, pH 7.5, 30°C, recombinant AAT1
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
formation of feruloyltyramine, half-maximal activity at pH 6.5 and pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
THT mRNA is expressed constitutively in all pepper organs
expression of tyramine-hydroxycinnamoyl transferase is highly induced upon Potato virus X infection in systemic leaves
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, no loss of activity for 2 months in the presence of 2-mercaptoethanol
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-80°C, no loss of activity for 4 months in the presence of 2-mercaptoethanol
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4°C, as ammonium sulfate paste, 10 mM mercaptoethanol, 24 h, 25% loss of activity
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4°C, as ammonium sulfate paste, 5 mM DTT, 10% loss of activity within 24 h
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4°C, no loss of activity for 14 days in the presence of 2-mercaptoethanol
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4°C, purified recombinant GST-tagged AAT1, in 50 mM Tris-Cl, pH 8.0, and 10 mM reduced glutathione, 4 weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
recombinant GST-tagged AAT1 from Escherichia coli by cell disruption through freeze-thaw cycles, and glutathione affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AAT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree of BAHD acyltransferases, expression of GST-tagged AAT1 in Escherichia coli strain Rosetta(DE3)pLysS
transformation of fusion product of THT and tyrosine decarboxylase in Agrobacterium tumefaciens
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F145Y
-
KM-value for tyramine is 2.3fold lower than wild-type value, Vmax is 3fold lower than wild-type value. Wild-type enzyme shows no activity with serotonin, mutant enzyms shows activity with serotonin
F145Y/Y147F
-
KM-value for tyramine is 2.3fold lower than wild-type value, Vmax is 4.2fold lower than wild-type value. Wild-type enzyme shows no activity with serotonin, mutant enzyms shows activity with serotonin
additional information
additional information
-
a series of chimeric genes is constructed by reciprocal exchange of DNA segments between the serotonin N-hydroxycinnamoyltransferase and tyramine N-hydroxycinnamoyltransferase cDNAs. Functional characterization of the recombinant chimeric proteins revealed that the amino acid residues 129 to 165 of serotonin N-hydroxycinnamoyltransferase and the corresponding residues 125 to 160 in tyramine N-hydroxycinnamoyltransferase are critical structural determinants for amine substrate specificity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.110)
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